## Abstract The conformational preferences of the 3,3‐disubstituted β‐amino acid residue, 1‐aminocyclohexaneacetic acid (β^3,3^Ac~6~c) have been investigated by determining the crystal structures of the parent amino acid, the hydrochloride derivative, 10 protected derivatives and di and tripeptides
β-Turn Analogues in Model αβ-Hybrid Peptides: Structural Characterization of Peptides Containing β2,2Ac6c and β3,3Ac6c Residues
✍ Scribed by Krishnayan Basuroy; Appavu Rajagopal; Dr. Srinivasarao Raghothama; Prof. Narayanaswamy Shamala; Prof. Padmanabhan Balaram
- Book ID
- 112006604
- Publisher
- John Wiley and Sons
- Year
- 2012
- Tongue
- English
- Weight
- 868 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1861-4728
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📜 SIMILAR VOLUMES
The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.
Two new glycosyl amino acids N'~-Fmoc-Ser[Ac4-fl-D-Galp-(1 ~ 3)-Ac2-a-D-GalN3P]-OPf p and N'~-Fmoc-Thr[Ac4-/3-D-Galp-(1 ~ 3)-Ac2-a-D-GalN3p]-OPf p were synthesized. Glycosylation of N'~-Fmoc-Ser-OPf p or N ~-Fmoc-Thr-OPfp with protected/3-o-Gal-( 1 -~ 3)-D-GaIN 3 donors afforded the glycosyl amino a
The dehydro-residue containing peptides N-Ac-dehydro-Phe-L-Leu-OCH3 ( I ) and N-Acdehydro-Phe-NorVal-OCH, (11) were synthesized by the usual workup procedures. The peptides crystallize from their solutions in methanol in space group P6,: ( I ) a = b = 12.528(2) A, c = 21.653(5) A; (11) a = b = 12.53